ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Chromodomain-helicase-DNA-binding protein 1

Intramolecular
Cysteine 411 and cysteine 436 L
Cysteine 1417 and cysteine 1461
Cysteine 411 and cysteine 421 L
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 1 between cysteines 411 and 436 (153 and 178 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2b2v
Structure name
crystal structure analysis of human chd1 chromodomains 1 and 2 bound to histone h3 resi 1-15 mek4
Structure deposition date
2005-09-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
67
Peptide accession
O14646
Residue number A
411
Residue number B
436
Peptide name
Chromodomain-helicase-DNA-binding protein 1

Ligandability

Cysteine 411 of Chromodomain-helicase-DNA-binding protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 436 of Chromodomain-helicase-DNA-binding protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 1 between cysteines 1417 and 1461 (14 and 58 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2n39
Structure name
nmr solution structure of a c-terminal domain of the chromodomain helicase dna-binding protein 1
Structure deposition date
2015-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
34
Peptide accession
O14646
Residue number A
1417
Residue number B
1461
Peptide name
Chromodomain-helicase-DNA-binding protein 1

Ligandability

Cysteine 1417 of Chromodomain-helicase-DNA-binding protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1461 of Chromodomain-helicase-DNA-binding protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 1 between cysteines 411 and 421 (153 and 163 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2b2y
Structure name
tandem chromodomains of human chd1
Structure deposition date
2005-09-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
92
Peptide accession
O14646
Residue number A
411
Residue number B
421
Peptide name
Chromodomain-helicase-DNA-binding protein 1

Ligandability

Cysteine 411 of Chromodomain-helicase-DNA-binding protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 421 of Chromodomain-helicase-DNA-binding protein 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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